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TBC1 domain family member 3C (TBC1D3C) is a primate-specific protein encoded by a gene that belongs to the TBC1 domain family. This protein contains a TBC (Tre2/Bub2/Cdc16) domain, typically characteristic of Rab GTPase-activating proteins involved in membrane trafficking and intracellular transport. However, despite possessing a TBC domain, TBC1D3C and its close homologs lack conserved catalytic residues and thus do not display classical Rab-GAP activity, distinguishing them from other TBC family members. TBC1D3C modulates signal transduction by interacting with GGA3 and ARF6, regulating macropinocytosis and possibly affecting actin remodeling in membrane ruffling events. The gene is highly duplicated and redundant in the human genome, with multiple paralogs and complex expression patterns, especially altered in prostate cancer compared to normal tissue. Therapeutically, the most consistent role is its contribution to cancer biology through the regulation of endocytosis and cell signaling
Not established for any drugs; mechanistic studies indicate TBC1D3C/related paralogs regulate macropinocytosis through ARF6-GGA3-RAB5 pathway
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